Graindorge J S, Senger B, Tritch D, Simos G, Fasiolo F
Role of Arc1p in the modulation of yeast glutamyl-tRNA synthetase activity Journal Article
In: Biochemistry, vol. 44, no. 4, pp. 1344-1352, 2005, ISBN: 15667228, (0006-2960 Journal Article).
Abstract | Links | BibTeX | Tags: FASIOLO Adenosine Triphosphate/chemistry/metabolism Amino Acid Sequence Aminoacylation Base Sequence Diphosphates/chemistry/metabolism Enzyme Activation Gene Expression Regulation, Fungal Glutamate-tRNA Ligase/isolation & purification/*metabolism Kinetics Molecular Sequence Data Peptide Fragments/chemistry/metabolism Protein Binding Protein Structure, Fungal/genetics/metabolism RNA, Genetic, Glu/genetics/metabolism RNA-Binding Proteins/*chemistry/isolation & purification/metabolism Research Support, Non-U.S. Gov't Saccharomyces cerevisiae/enzymology/genetics/metabolism Saccharomyces cerevisiae Proteins/*chemistry/isolation & purification/metabolism Transcription, Tertiary RNA, Transfer, Unité ARN
@article{,
title = {Role of Arc1p in the modulation of yeast glutamyl-tRNA synthetase activity},
author = {J S Graindorge and B Senger and D Tritch and G Simos and F Fasiolo},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=15667228},
isbn = {15667228},
year = {2005},
date = {2005-01-01},
journal = {Biochemistry},
volume = {44},
number = {4},
pages = {1344-1352},
abstract = {Yeast methionyl-tRNA synthetase (MetRS) and glutamyl-tRNA synthetase (GluRS) possess N-terminal extensions that bind the cofactor Arc1p in trans. The strength of GluRS-Arc1p interaction is high enough to allow copurification of the two macromolecules in a 1:1 ratio, in contrast to MetRS. Deletion analysis from the C-terminal end of the GluRS appendix combined with previous N-terminal deletions of GluRS allows restriction of the Arc1p binding site to the 110-170 amino acid region of GluRS. This region has been shown to correspond to a novel protein-protein interaction domain present in both GluRS and Arc1p but not in MetRS [Galani, K., Grosshans, H., Deinert, K., Hurt, E. C., and Simos, G. (2001) EMBO J. 20, 6889-6898]. The GluRS apoenzyme fails to show significant kinetics of tRNA aminoacylation and charges unfractionated yeast tRNA at a level 10-fold reduced compared to Arc1p-bound GluRS. The K(m) values for tRNA(Glu) measured in the ATP-PP(i) exchange were similar for the two forms of GluRS, whereas k(cat) is increased 2-fold in the presence of Arc1p. Band-shift analysis revealed a 100-fold increase in tRNA binding affinity when Arc1p is bound to GluRS. This increase requires the RNA binding properties of the full-length Arc1p since Arc1p N domain leaves the K(d) of GluRS for tRNA unchanged. Transcripts of yeast tRNA(Glu) were poor substrates for measuring tRNA aminoacylation and could not be used to clarify whether Arc1p has a specific effect on the tRNA charging reaction.},
note = {0006-2960
Journal Article},
keywords = {FASIOLO Adenosine Triphosphate/chemistry/metabolism Amino Acid Sequence Aminoacylation Base Sequence Diphosphates/chemistry/metabolism Enzyme Activation Gene Expression Regulation, Fungal Glutamate-tRNA Ligase/isolation & purification/*metabolism Kinetics Molecular Sequence Data Peptide Fragments/chemistry/metabolism Protein Binding Protein Structure, Fungal/genetics/metabolism RNA, Genetic, Glu/genetics/metabolism RNA-Binding Proteins/*chemistry/isolation & purification/metabolism Research Support, Non-U.S. Gov't Saccharomyces cerevisiae/enzymology/genetics/metabolism Saccharomyces cerevisiae Proteins/*chemistry/isolation & purification/metabolism Transcription, Tertiary RNA, Transfer, Unité ARN},
pubstate = {published},
tppubtype = {article}
}